5bns: Difference between revisions
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New page: '''Unreleased structure''' The entry 5bns is ON HOLD Authors: Kazmirski, S.L., McKinney, D.C. Description: E. coli Fabh with small molecule inhibitor 2 [[Category: Unreleased Structure... |
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==E. coli Fabh with small molecule inhibitor 2== | |||
<StructureSection load='5bns' size='340' side='right'caption='[[5bns]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5bns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BNS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4VM:1-{5-[2-FLUORO-5-(HYDROXYMETHYL)PHENYL]PYRIDIN-2-YL}-N-(QUINOLIN-6-YLMETHYL)PIPERIDINE-4-CARBOXAMIDE'>4VM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bns OCA], [https://pdbe.org/5bns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bns RCSB], [https://www.ebi.ac.uk/pdbsum/5bns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bns ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815] | |||
==See Also== | |||
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Kazmirski SL]] | |||
[[Category: McKinney DC]] |
Latest revision as of 15:17, 6 March 2024
E. coli Fabh with small molecule inhibitor 2E. coli Fabh with small molecule inhibitor 2
Structural highlights
FunctionFABH_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815] See Also |
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